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Results 1 - 10 of 23 > >>
EC Number Natural Substrates Commentary (Nat. Sub.)
Display the word mapDisplay the reaction diagram Show all sequences 3.4.18.1Proteins + H2O -
Display the word mapDisplay the reaction diagram Show all sequences 3.4.18.1more active cathepsin X mediates the function of beta2 integrin receptors during cell adhesion. It could also be involved in other processes associated with beta2 integrin receptors such as phagocytosis and T cell activation
Display the word mapDisplay the reaction diagram Show all sequences 3.4.18.1more cathepsin X acts as a monocarboxypepidase and has a strict positional and narrower substrate specificity relative to the other human cathepsins
Display the word mapDisplay the reaction diagram Show all sequences 3.4.18.1more cathepsin X binds to the membrane lectin endoplasmic reticulum Golgi intermediate compartment protein-53, ERGIC-53, involving the soluble luminal interaction partner multiple coagulation factor deficiency protein 2, MCFD2, which form a cargo receptor complex in the early secretory pathway, but is dispensable for enzyme binding, overview
Display the word mapDisplay the reaction diagram Show all sequences 3.4.18.1profilin + H2O cathepsin X cleaves profilin 1 C-terminal Tyr139 and influences clathrin-mediated endocytosis. Tyr139 is important for proper function of profilin 1 as a tumor suppressor. Cleaving off Tyr139 prevents the binding of clathrin, a poly-L-proline ligand involved in endocytosis
Display the word mapDisplay the reaction diagram Show all sequences 3.4.18.1lymphocyte function associated antigen-1 + H2O cathepsin X cleaves the beta2 cytoplasmic tail of LFA-1 inducing the intermediate affinity form of LFA-1 and alpha-actinin-1 binding. Cleavage by cathepsin X of the amino acid residues S769, E768 and A767 from the C-terminal of the b2 cytoplasmic tail of LFA-1 promotes binding of the actin-binding protein a-actinin-1
Display the word mapDisplay the reaction diagram Show all sequences 3.4.18.1alpha-enolase + H2O cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
Display the word mapDisplay the reaction diagram Show all sequences 3.4.18.1gamma-enolase + H2O cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
Display the word mapDisplay the reaction diagram Show all sequences 3.4.18.1more cathepsin X is an important regulator of LFA-1 activity, and cathepsin X-upregulated Jurkat T cells exhibit increased homotypic aggregation, cathepsin X induces polarized migration-associated morphology in Jurkat T cells, overview
Display the word mapDisplay the reaction diagram Show all sequences 3.4.18.1more cathepsin X plays a role not only in the chronic inflammation of gastric mucosa but also in the tumourigenesis of gastric cancer
Results 1 - 10 of 23 > >>